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Conserved domains on  [gi|25143331|ref|NP_490666|]
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CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase [Caenorhabditis elegans]

Protein Classification

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase( domain architecture ID 10173612)

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase catalyzes the committed step in the biosynthesis of acidic phospholipids

EC:  2.7.8.5
Gene Ontology:  GO:0032049|GO:0008444|GO:0005509|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 242-417 9.14e-82

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


:

Pssm-ID: 197235  Cd Length: 186  Bit Score: 250.19  E-value: 9.14e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 242 TWIYPVLQMGLLGIHQEFEFLQKLFSLKNPELKMTMASGYFNFIRDYEESILkEGDYHLDILTASPFANGFFESNGFSKY 321
Cdd:cd09137   1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLL-NSSANLDVLTASPEANGFYGSKGVSGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 322 IPPLYSNISDQFLRKREINGRL-NVKMFEYRREEWTFHAKGLWAEHNNQ---LMTLIGSSNYGYRSVHRDLEAQVMVVTR 397
Cdd:cd09137  80 IPPAYTYIARQFLKRVRKNGKQpRIKLFEYKRPGWTFHAKGLWIYLPGTdlpSLTLIGSSNYGYRSVHRDLEAQFLIVTN 159

                       170       180
                ....*....|....*....|
gi 25143331 398 NPTLIDRLKDEKNLLFEYSS 417
Cdd:cd09137 160 NPKLQQQLKEELENLFEYSK 179
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 17-182 5.75e-81

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


:

Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 247.46  E-value: 5.75e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  17 DLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSEK-SEIEVTILLDFLRGTRTNSSGESSVTV 95
Cdd:cd09135   1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERnPNLKVSILLDYLRGTRGEPNSRTASLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  96 LKP---ISEKSKIYLFHTPELSGLVKRVLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTNRTDRYFLFRNCKPLA 172
Cdd:cd09135  81 LPLlklFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIENCPELA 160

                       170
                ....*....|
gi 25143331 173 DFFHEIINVV 182
Cdd:cd09135 161 DFYHDLIKAV 170
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 242-417 9.14e-82

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197235  Cd Length: 186  Bit Score: 250.19  E-value: 9.14e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 242 TWIYPVLQMGLLGIHQEFEFLQKLFSLKNPELKMTMASGYFNFIRDYEESILkEGDYHLDILTASPFANGFFESNGFSKY 321
Cdd:cd09137   1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLL-NSSANLDVLTASPEANGFYGSKGVSGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 322 IPPLYSNISDQFLRKREINGRL-NVKMFEYRREEWTFHAKGLWAEHNNQ---LMTLIGSSNYGYRSVHRDLEAQVMVVTR 397
Cdd:cd09137  80 IPPAYTYIARQFLKRVRKNGKQpRIKLFEYKRPGWTFHAKGLWIYLPGTdlpSLTLIGSSNYGYRSVHRDLEAQFLIVTN 159

                       170       180
                ....*....|....*....|
gi 25143331 398 NPTLIDRLKDEKNLLFEYSS 417
Cdd:cd09137 160 NPKLQQQLKEELENLFEYSK 179
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 17-182 5.75e-81

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 247.46  E-value: 5.75e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  17 DLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSEK-SEIEVTILLDFLRGTRTNSSGESSVTV 95
Cdd:cd09135   1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERnPNLKVSILLDYLRGTRGEPNSRTASLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  96 LKP---ISEKSKIYLFHTPELSGLVKRVLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTNRTDRYFLFRNCKPLA 172
Cdd:cd09135  81 LPLlklFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIENCPELA 160

                       170
                ....*....|
gi 25143331 173 DFFHEIINVV 182
Cdd:cd09135 161 DFYHDLIKAV 170
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
7-414 8.10e-23

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 100.27  E-value: 8.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331    7 ELPGIPIDPQDLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRE-RSEKSEIEVTILLDFLRGTRT 85
Cdd:PRK09428  16 QLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDALYQaKQQNPELDIKVLVDWHRAQRG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331   86 NSSGESSVTVLKPISEKSKIYLFHTPELSGlvkrvLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTN----RTDR 161
Cdd:PRK09428  96 LIGAAASNTNADWYCEMAQEYPGVDIPVYG-----VPVNTREALGVLHLKGFIIDDTVLYSGASLNNVYLHQhdkyRYDR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  162 YFLFRNcKPLADFF-----HEIINVVADSSFIVENEQLVPSPKCDVhpylgsaHLYREMLKTRvnrvieKYKESRKTSSN 236
Cdd:PRK09428 171 YHLIRN-AELADSMvnfiqQNLLNSPAVNRLDQPNRPKTKEIKNDI-------RQFRQRLRDA------AYQFQGQANND 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  237 CMSadtwIYPVLQMG---LL--GIHQEFEFLQKlfslknpelKMTMASGYFNFIRdyeeSILKEGDYHL------DILTA 305
Cdd:PRK09428 237 ELS----VTPLVGLGkknLLnkTIFHLMASAEQ---------KLTICTPYFNLPA----ILVRNIIRLLrrgkkvEIIVG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  306 SPFANGFfesngfskYIPP------------LYSNISDQFLRKRE--I-NGRLNVKMfeYRREEWTFHAKGLWAEHNNQL 370
Cdd:PRK09428 300 DKTANDF--------YIPPdepfkiigalpyLYEINLRRFAKRLQyyIdNGQLNVRL--WKDGDNSYHLKGIWVDDRWML 369

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 25143331  371 MTligSSNYGYRSVHRDLEaqvmvvtrNPTLIDrlkDEKNLLFE 414
Cdd:PRK09428 370 LT---GNNLNPRAWRLDLE--------NALLIH---DPKQELAE 399
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 12-446 6.48e-12

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 66.50  E-value: 6.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  12 PIDPQDLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSeKSEIEVTILLDFLrGTRTNSSgeS 91
Cdd:COG1502  11 LVGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAA-RRGVKVRVLLDGI-GSRALNR--D 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  92 SVTVLKpiSEKSKIYLFHTPelsglvkRVLPQRADeiiGLQHMKLYIFDDNV-LISGANLSDSYFTN------RTDRYFL 164
Cdd:COG1502  87 FLRRLR--AAGVEVRLFNPV-------RLLFRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfgpWRDTHVR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 165 FRNckP----LADFFHEIINVVADSSFIVENeqlvPSPKCDVHPYLGSAHLYREMLKTRVNRVIEkykesrktssncmSA 240
Cdd:COG1502 155 IEG--PavadLQAVFAEDWNFATGEALPFPE----PAGDVRVQVVPSGPDSPRETIERALLAAIA-------------SA 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 241 DTWIYpvlqmgllgihqefeflqklfslknpelkmtMASGYFNF---IRDYEESILKEGdYHLDILTaSPFANGFFESNG 317
Cdd:COG1502 216 RRRIY-------------------------------IETPYFVPdrsLLRALIAAARRG-VDVRILL-PAKSDHPLVHWA 262

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 318 FSKYIPPLysnisdqflrkreinGRLNVKMFEYRReeWTFHAKGLWAEHNnqlMTLIGSSNYGYRSVHRDLEaqVMVVTR 397
Cdd:COG1502 263 SRSYYEEL---------------LEAGVRIYEYEP--GFLHAKVMVVDDE---WALVGSANLDPRSLRLNFE--VNLVIY 320

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 25143331 398 NPTLIDRLKDEKNLLFEYSSILDMAALQQPehHIPPLVRVISRLIRSFL 446
Cdd:COG1502 321 DPEFAAQLRARFEEDLAHSREVTLEEWRKR--PLRRLRERLARLLSPLL 367
PLDc_2 pfam13091
PLD-like domain;
327-408 3.25e-06

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 46.13  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331   327 SNISDQFLRKREINGRL------NVKMFEYRREEWTFHAKGLWAEHNnqlMTLIGSSNYGYRSVHRDLEAqvMVVTRNPT 400
Cdd:pfam13091  45 SNKDDAGGPKKASLKELrsllraGVEIREYQSFLRSMHAKFYIIDGK---TVIVGSANLTRRALRLNLEN--NVVIKDPE 119


                  ....*...
gi 25143331   401 LIDRLKDE 408
Cdd:pfam13091 120 LAQELEKE 127
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 130-154 3.77e-03

Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, aspartic acid, and/or asparagine residues which may contribute to the active site. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 34.67  E-value: 3.77e-03
                           10        20
                   ....*....|....*....|....*.
gi 25143331    130 GLQHMKLYIFDD-NVLISGANLSDSY 154
Cdd:smart00155   3 GVLHTKLMIVDDeIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 242-417 9.14e-82

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197235  Cd Length: 186  Bit Score: 250.19  E-value: 9.14e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 242 TWIYPVLQMGLLGIHQEFEFLQKLFSLKNPELKMTMASGYFNFIRDYEESILkEGDYHLDILTASPFANGFFESNGFSKY 321
Cdd:cd09137   1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLL-NSSANLDVLTASPEANGFYGSKGVSGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 322 IPPLYSNISDQFLRKREINGRL-NVKMFEYRREEWTFHAKGLWAEHNNQ---LMTLIGSSNYGYRSVHRDLEAQVMVVTR 397
Cdd:cd09137  80 IPPAYTYIARQFLKRVRKNGKQpRIKLFEYKRPGWTFHAKGLWIYLPGTdlpSLTLIGSSNYGYRSVHRDLEAQFLIVTN 159

                       170       180
                ....*....|....*....|
gi 25143331 398 NPTLIDRLKDEKNLLFEYSS 417
Cdd:cd09137 160 NPKLQQQLKEELENLFEYSK 179
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 17-182 5.75e-81

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 247.46  E-value: 5.75e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  17 DLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSEK-SEIEVTILLDFLRGTRTNSSGESSVTV 95
Cdd:cd09135   1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERnPNLKVSILLDYLRGTRGEPNSRTASLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  96 LKP---ISEKSKIYLFHTPELSGLVKRVLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTNRTDRYFLFRNCKPLA 172
Cdd:cd09135  81 LPLlklFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIENCPELA 160

                       170
                ....*....|
gi 25143331 173 DFFHEIINVV 182
Cdd:cd09135 161 DFYHDLIKAV 170
PLDc_CDP-OH_P_transf_II_1 cd09102
Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 19-182 2.04e-39

Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197201 [Multi-domain]  Cd Length: 168  Bit Score: 139.65  E-value: 2.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  19 EILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSEKS-EIEVTILLDFLRGTRTNSSGES-SVTVL 96
Cdd:cd09102   3 RFLGSPAEFKTQIIELIRNAKRRVYVASLYWGKDEAGQEILDEIYSVKQENpNLDVSVLIDWHRAQRNLLGSETkSATNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  97 KPISEKSKIYLFHTPELSGLVKRVLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTNRTDRYFLFRNCKPLADFFH 176
Cdd:cd09102  83 DWYCEQRQTSQLHLLPDDGN*FFGVPINTNEVFGVLHVKGYVFDDTVLLSGANLSNVYFHYRYDRYVKITHGAELADS*V 162


                ....*.
gi 25143331 177 EIINVV 182
Cdd:cd09102 163 NLINAY 168
PLDc_CDP-OH_P_transf_II_2 cd09103
Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 242-419 1.54e-24

Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197202 [Multi-domain]  Cd Length: 184  Bit Score: 99.99  E-value: 1.54e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 242 TWIYPVLQMGLLG------IHQEFEFLQKlfslknpelKMTMASGYFNFIRDYEESI---LKEGdYHLDILTASPFANGF 312
Cdd:cd09103   1 LSITPLVGLGKRGnilnrtIEQLITSAES---------KIILCTPYFNLPQALMRDIlrlLKRG-VKVEIIVGDKTANDF 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 313 F----ESNGFSKYIPPLYSNISDQFLRKREI---NGRLNVKMfeYRREEWTFHAKGLWAEhnnQLMTLIGSSNYGYRSVH 385
Cdd:cd09103  71 YippeEPFKVIGALPYLYEINLRRFAKRLQKyidQGQLNVRL--WKDGDNSFHLKGIWVD---DRYTLLTGNNLNPRAWR 145

                       170       180       190
                ....*....|....*....|....*....|....
gi 25143331 386 RDLEAQVMVVTRNPTLIDRLKDEKNLLFEYSSIL 419
Cdd:cd09103 146 LDLENGLLIHDPQKQLQQQLEKELEQILLHTTRI 179
PLDc_PSS_G_neg_1 cd09134
Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; ...
 8-173 3.47e-24

Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 1, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197232 [Multi-domain]  Cd Length: 173  Bit Score: 98.48  E-value: 3.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331   8 LPGIPIDPQDLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAI-RERSEKSEIEVTILLDFLRGTRT- 85
Cdd:cd09134   1 LPKIPQQPEDIDVLYSPKDFRARLLELISNAKKRIYIVALYLEDDEAGREILDALyEAKANNPGLDIKVLVDWHRAQRGl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  86 ----NSSGESSVTVLKPISEKSKIYLFHTPelsglVKRvlpqraDEIIGLQHMKLYIFDDNVLISGANLSDSYFTN---- 157
Cdd:cd09134  81 igakKSLGNADWYRKIAQRYGHDVPIYGVP-----VKT------RELFGVLHLKGFIIDDTVLYSGASLNNVYLHQfdky 149

                       170
                ....*....|....*.
gi 25143331 158 RTDRYFLFRNcKPLAD 173
Cdd:cd09134 150 RYDRYHLIYN-PELAD 164
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
7-414 8.10e-23

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 100.27  E-value: 8.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331    7 ELPGIPIDPQDLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRE-RSEKSEIEVTILLDFLRGTRT 85
Cdd:PRK09428  16 QLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDALYQaKQQNPELDIKVLVDWHRAQRG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331   86 NSSGESSVTVLKPISEKSKIYLFHTPELSGlvkrvLPQRADEIIGLQHMKLYIFDDNVLISGANLSDSYFTN----RTDR 161
Cdd:PRK09428  96 LIGAAASNTNADWYCEMAQEYPGVDIPVYG-----VPVNTREALGVLHLKGFIIDDTVLYSGASLNNVYLHQhdkyRYDR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  162 YFLFRNcKPLADFF-----HEIINVVADSSFIVENEQLVPSPKCDVhpylgsaHLYREMLKTRvnrvieKYKESRKTSSN 236
Cdd:PRK09428 171 YHLIRN-AELADSMvnfiqQNLLNSPAVNRLDQPNRPKTKEIKNDI-------RQFRQRLRDA------AYQFQGQANND 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  237 CMSadtwIYPVLQMG---LL--GIHQEFEFLQKlfslknpelKMTMASGYFNFIRdyeeSILKEGDYHL------DILTA 305
Cdd:PRK09428 237 ELS----VTPLVGLGkknLLnkTIFHLMASAEQ---------KLTICTPYFNLPA----ILVRNIIRLLrrgkkvEIIVG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  306 SPFANGFfesngfskYIPP------------LYSNISDQFLRKRE--I-NGRLNVKMfeYRREEWTFHAKGLWAEHNNQL 370
Cdd:PRK09428 300 DKTANDF--------YIPPdepfkiigalpyLYEINLRRFAKRLQyyIdNGQLNVRL--WKDGDNSYHLKGIWVDDRWML 369

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 25143331  371 MTligSSNYGYRSVHRDLEaqvmvvtrNPTLIDrlkDEKNLLFE 414
Cdd:PRK09428 370 LT---GNNLNPRAWRLDLE--------NALLIH---DPKQELAE 399
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 12-446 6.48e-12

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 66.50  E-value: 6.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  12 PIDPQDLEILDTPTRFYEKLLELTASTERRLALCSLYLGEGDLEKNLIAAIRERSeKSEIEVTILLDFLrGTRTNSSgeS 91
Cdd:COG1502  11 LVGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAA-RRGVKVRVLLDGI-GSRALNR--D 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  92 SVTVLKpiSEKSKIYLFHTPelsglvkRVLPQRADeiiGLQHMKLYIFDDNV-LISGANLSDSYFTN------RTDRYFL 164
Cdd:COG1502  87 FLRRLR--AAGVEVRLFNPV-------RLLFRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfgpWRDTHVR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 165 FRNckP----LADFFHEIINVVADSSFIVENeqlvPSPKCDVHPYLGSAHLYREMLKTRVNRVIEkykesrktssncmSA 240
Cdd:COG1502 155 IEG--PavadLQAVFAEDWNFATGEALPFPE----PAGDVRVQVVPSGPDSPRETIERALLAAIA-------------SA 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 241 DTWIYpvlqmgllgihqefeflqklfslknpelkmtMASGYFNF---IRDYEESILKEGdYHLDILTaSPFANGFFESNG 317
Cdd:COG1502 216 RRRIY-------------------------------IETPYFVPdrsLLRALIAAARRG-VDVRILL-PAKSDHPLVHWA 262

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 318 FSKYIPPLysnisdqflrkreinGRLNVKMFEYRReeWTFHAKGLWAEHNnqlMTLIGSSNYGYRSVHRDLEaqVMVVTR 397
Cdd:COG1502 263 SRSYYEEL---------------LEAGVRIYEYEP--GFLHAKVMVVDDE---WALVGSANLDPRSLRLNFE--VNLVIY 320

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 25143331 398 NPTLIDRLKDEKNLLFEYSSILDMAALQQPehHIPPLVRVISRLIRSFL 446
Cdd:COG1502 321 DPEFAAQLRARFEEDLAHSREVTLEEWRKR--PLRRLRERLARLLSPLL 367
PLDc_2 pfam13091
PLD-like domain;
327-408 3.25e-06

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 46.13  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331   327 SNISDQFLRKREINGRL------NVKMFEYRREEWTFHAKGLWAEHNnqlMTLIGSSNYGYRSVHRDLEAqvMVVTRNPT 400
Cdd:pfam13091  45 SNKDDAGGPKKASLKELrsllraGVEIREYQSFLRSMHAKFYIIDGK---TVIVGSANLTRRALRLNLEN--NVVIKDPE 119


                  ....*...
gi 25143331   401 LIDRLKDE 408
Cdd:pfam13091 120 LAQELEKE 127
PLDc_PSS_G_neg_2 cd09136
Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; ...
 274-443 5.20e-06

Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 2, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197234  Cd Length: 215  Bit Score: 47.21  E-value: 5.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 274 KMTMASGYFNF----IRDYEeSILKEGdYHLDILTASPFANGFF--ESNGFSKY--IPPLYSNISDQFLRKRE--I-NGR 342
Cdd:cd09136  30 ELIICTPYFNLprslVRDIA-RLLKRG-VKVEIIVGDKTANDFYipPEEPFKTIgaLPYLYEINLRRFAKRLQkyIdNGQ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 343 LNVKMfeYRREEWTFHAKGLWAEHNNQLMTligSSNYGYRSVHRDLEAQVMVVTRNPTLIDRLKDEKNLLFEYSSILD-M 421
Cdd:cd09136 108 LNVRL--WKDGNNSFHLKGIWVDDRYHLLT---GNNLNPRAWRLDLENGLLIHDPQGQLKAQFEKELEQILAHTTRIKhY 182

                       170       180
                ....*....|....*....|..
gi 25143331 422 AALQQPEHHIPPLVRVISRLIR 443
Cdd:cd09136 183 SQLESIADYPEKVQKLLRRIRR 204
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 344-443 1.24e-04

Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase ybhO and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli CL synthase. The prototype of this subfamily is Escherichia coli CL synthase ybhO specified by the f413 (ybhO) gene. ybhO is a membrane-bound protein that catalyzes the formation of cardiolipin (CL) by transferring phosphatidyl group between two phosphatidylglycerol molecules. It can also catalyze phosphatidyl group transfer to water to form phosphatidate. In contrast to the Escherichia coli CL synthase encoded by the cls gene (EcCLS), ybhO does not hydrolyze CL. Moreover, ybhO lacks an N-terminal segment encoded by Escherichia coli cls, which makes ybhO easy to denature. The monomer of ybhO consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. ybhO can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily.


Pssm-ID: 197256 [Multi-domain]  Cd Length: 170  Bit Score: 42.53  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331 344 NVKMFEYRREewTFHAK-----GLWAehnnqlmtLIGSSNYGYRSVHRDLEAqvMVVTRNPTLIDRLKDeknlLFEyssi 418
Cdd:cd09159  82 GVRIFEYQPS--MLHAKtavidGDWA--------TVGSSNLDPRSLRLNLEA--NLVVEDPAFAAQLEE----LFE---- 141

                        90       100
                ....*....|....*....|....*....
gi 25143331 419 LDMAALQQ--PE--HHIPPLVRVISRLIR 443
Cdd:cd09159 142 EDLARSREitLEewRRRPLWQRLLEWLAY 170
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 31-165 3.74e-04

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 40.19  E-value: 3.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143331  31 LLELTASTERRLALCSLYLGEG---DLEKNLIAAIrerseKSEIEVTILLDflrgtRTNSSGESSVTVLKPISEKSKIYL 107
Cdd:cd00138   3 LLELLKNAKESIFIATPNFSFNsadRLLKALLAAA-----ERGVDVRLIID-----KPPNAAGSLSAALLEALLRAGVNV 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143331 108 fhtpelsglvkrVLPQRADEIIGLQHMKLYIFDDN-VLISGANLSDSYFTNRTDRYFLF 165
Cdd:cd00138  73 ------------RSYVTPPHFFERLHAKVVVIDGEvAYVGSANLSTASAAQNREAGVLV 119
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 130-154 3.77e-03

Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, aspartic acid, and/or asparagine residues which may contribute to the active site. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 34.67  E-value: 3.77e-03
                           10        20
                   ....*....|....*....|....*.
gi 25143331    130 GLQHMKLYIFDD-NVLISGANLSDSY 154
Cdd:smart00155   3 GVLHTKLMIVDDeIAYIGSANLDGRS 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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